A likely role for a novel PH-domain containing protein, PEPP2, in connecting membrane and cytoskeleton

作者：Zou, Yi^*; Zhong, Wenping

来源：Biocell, 2012, 36(3): 127-132.

• microtubule
• membrane
• phosphoinositide
• microviscosity
• wortmannin

PH domains (pleckstrin homology) are well known to bind membrane phosphoinositides with different specificities and direct PH domain-containing proteins to discrete subcellular apartments with assistances of alternative binding partners. PH domain-containing proteins are found to be involved in a wide range of cellular events, including signalling, cytoskeleton rearrangement and vesicular trafficking. Here we showed that a novel PH domain-containing protein, PEPP2, displayed moderate phosphoinositide binding specificity. Full length PEPP2 associated with both plasma membrane and microtubules. The membrane-associated PEPP2 nucleated at cell-cell contacts and the leading edge of migrating cells. Overexpression of PEPP2 increased membrane microviscosity, indicating a potential role of PEPP2 in regulating function of membrane and microtubules.

• 出版日期2012-12
• 单位暨南大学